POPDC1 Scaffolds a Complex of Adenylyl Cyclase 9 and the Potassium Channel TREK-1 in Heart

ABSTRACT: The establishment of macromolecular complexes by scaffolding proteins is key to local production of cAMP by anchored adenylyl cyclase (AC) and the subsequent cAMP signaling necessary for cardiac functions. We identify a novel AC scaffold, the Popeye domain-containing (POPDC) protein. The POPDC family of proteins are important for cardiac pacemaking and conduction, due in part to their cAMP-dependent binding and regulation of TREK-1 potassium channels. We show that TREK-1 binds the AC9:POPDC1 complex and co-purifies in a POPDC1-dependent manner with AC9 activity in heart. Although the AC9:POPDC1 interaction is cAMP independent, TREK-1 association with AC9 and POPDC1 is reduced upon stimulation of the β-adrenergic receptor (βAR). AC9 activity is required for βAR reduction of TREK-1 complex f

SUBMITTER: Tanya, A. Baldwin 

PROVIDER: S-SCDT-10_15252-EMBR_202255208 | biostudies-other |

REPOSITORIES: biostudies-other